ID ENO_POLSJ Reviewed; 427 AA. AC Q128E4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 29-MAY-2024, entry version 107. DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318}; DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318}; GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=Bpro_3184; OS Polaromonas sp. (strain JS666 / ATCC BAA-500). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=296591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS666 / ATCC BAA-500; RX PubMed=18723656; DOI=10.1128/aem.00197-08; RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S., RA Stothard P., Coleman N.V.; RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of RT relevance to biotechnology."; RL Appl. Environ. Microbiol. 74:6405-6416(2008). CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2- CC PG) into phosphoenolpyruvate (PEP). It is essential for the degradation CC of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, CC ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00318}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; CC Note=Binds a second Mg(2+) ion via substrate during catalysis. CC {ECO:0000255|HAMAP-Rule:MF_00318}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. CC Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface CC {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are CC present in both the cytoplasm and on the cell surface. CC {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000316; ABE45098.1; -; Genomic_DNA. DR RefSeq; WP_011484093.1; NC_007948.1. DR AlphaFoldDB; Q128E4; -. DR SMR; Q128E4; -. DR STRING; 296591.Bpro_3184; -. DR KEGG; pol:Bpro_3184; -. DR eggNOG; COG0148; Bacteria. DR HOGENOM; CLU_031223_2_1_4; -. DR OrthoDB; 9804716at2; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000001983; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd03313; enolase; 1. DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR036849; Enolase-like_C_sf. DR InterPro; IPR029017; Enolase-like_N. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR NCBIfam; TIGR01060; eno; 1. DR PANTHER; PTHR11902; ENOLASE; 1. DR PANTHER; PTHR11902:SF1; ENOLASE; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR SFLD; SFLDF00002; enolase; 1. DR SFLD; SFLDG00178; enolase; 1. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome; KW Secreted. FT CHAIN 1..427 FT /note="Enolase" FT /id="PRO_0000267071" FT ACT_SITE 205 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT ACT_SITE 337 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 163 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 285 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 312 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 337 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 366 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 367 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 388 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" SQ SEQUENCE 427 AA; 45678 MW; C8BBCB883A426284 CRC64; MSAIVDIVGR EILDSRGNPT VECDVLLESG VMGRAAVPSG ASTGSREAIE LRDGDKSRYL GKGVLKAVEH INTEISEAVL GLDASEQAFL DRTLIDLDGT DNKSRLGANA TLAVSMAVAR AAAEEAGLPL YRYFGGSGAM QMPVPMMNVV NGGAHANNNL DLQELMIIPI GAPSFREAVR YGAEVFHALK KILHDKGMSV AVGDEGGFAP NVPSHEAAIQ MILEAIDKAG YVAGEQIALG LDCAASEFYK DGKYVLAGEG LSLDATEWTN ILATWVDKYP IISIEDGMAE GDWDGWKILT ERLGKQVQLV GDDLFVTNTK ILKEGIDKHI ANSILIKINQ IGTLTETFAA IEMAKRAGYT AVISHRSGET EDSTIADIAV GTNAGQIKTG SLSRSDRMAK YNQLLRIEED LGDIATYPGR AAFYNLR //